The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant
The class III anaerobic ribonucleotide reductases (RNRs) studied to date couple the reduction of ribonucleotides to deoxynucleotides with the oxidation of formate to CO[subscript 2]. Here we report the cloning and heterologous expression of the Neisseria bacilliformis class III RNR and show that it...
| Main Authors: | , , , , , |
|---|---|
| Other Authors: | |
| Format: | Article |
| Language: | en_US |
| Published: |
National Academy of Sciences (U.S.)
2015
|
| Online Access: | http://hdl.handle.net/1721.1/95768 https://orcid.org/0000-0001-5486-2755 https://orcid.org/0000-0002-8683-3593 https://orcid.org/0000-0001-8076-4489 |
| _version_ | 1826196508160032768 |
|---|---|
| author | Wei, Yifeng Funk, Michael Andrew Rosado, Leonardo A. Baek, Jiyeon Stubbe, JoAnne Drennan, Catherine L |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Wei, Yifeng Funk, Michael Andrew Rosado, Leonardo A. Baek, Jiyeon Stubbe, JoAnne Drennan, Catherine L |
| author_sort | Wei, Yifeng |
| collection | MIT |
| description | The class III anaerobic ribonucleotide reductases (RNRs) studied to date couple the reduction of ribonucleotides to deoxynucleotides with the oxidation of formate to CO[subscript 2]. Here we report the cloning and heterologous expression of the Neisseria bacilliformis class III RNR and show that it can catalyze nucleotide reduction using the ubiquitous thioredoxin/thioredoxin reductase/NADPH system. We present a structural model based on a crystal structure of the homologous Thermotoga maritima class III RNR, showing its architecture and the position of conserved residues in the active site. Phylogenetic studies suggest that this form of class III RNR is present in bacteria and archaea that carry out diverse types of anaerobic metabolism. |
| first_indexed | 2024-09-23T10:28:04Z |
| format | Article |
| id | mit-1721.1/95768 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T10:28:04Z |
| publishDate | 2015 |
| publisher | National Academy of Sciences (U.S.) |
| record_format | dspace |
| spelling | mit-1721.1/957682022-09-30T21:18:49Z The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant Wei, Yifeng Funk, Michael Andrew Rosado, Leonardo A. Baek, Jiyeon Stubbe, JoAnne Drennan, Catherine L Massachusetts Institute of Technology. Department of Biology Massachusetts Institute of Technology. Department of Chemistry Wei, Yifeng Funk, Michael Andrew Rosado, Leonardo A. Baek, Jiyeon Drennan, Catherine L. Stubbe, JoAnne The class III anaerobic ribonucleotide reductases (RNRs) studied to date couple the reduction of ribonucleotides to deoxynucleotides with the oxidation of formate to CO[subscript 2]. Here we report the cloning and heterologous expression of the Neisseria bacilliformis class III RNR and show that it can catalyze nucleotide reduction using the ubiquitous thioredoxin/thioredoxin reductase/NADPH system. We present a structural model based on a crystal structure of the homologous Thermotoga maritima class III RNR, showing its architecture and the position of conserved residues in the active site. Phylogenetic studies suggest that this form of class III RNR is present in bacteria and archaea that carry out diverse types of anaerobic metabolism. Singapore. Agency for Science, Technology and Research National Science Foundation (U.S.). Graduate Research Fellowship Program (Grant 0645960) United States. Dept. of Energy. Office of Basic Energy Sciences (Contract DE-AC02-06CH11357) National Institutes of Health (U.S.) (Grant GM29595) 2015-03-03T19:46:32Z 2015-03-03T19:46:32Z 2014-08 2014-07 Article http://purl.org/eprint/type/JournalArticle 0027-8424 1091-6490 http://hdl.handle.net/1721.1/95768 Wei, Y., M. A. Funk, L. A. Rosado, J. Baek, C. L. Drennan, and J. Stubbe. “The Class III Ribonucleotide Reductase from Neisseria Bacilliformis Can Utilize Thioredoxin as a Reductant.” Proceedings of the National Academy of Sciences 111, no. 36 (August 25, 2014): E3756–E3765. https://orcid.org/0000-0001-5486-2755 https://orcid.org/0000-0002-8683-3593 https://orcid.org/0000-0001-8076-4489 en_US http://dx.doi.org/10.1073/pnas.1414396111 Proceedings of the National Academy of Sciences of the United States of America Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf National Academy of Sciences (U.S.) National Academy of Sciences (U.S.) |
| spellingShingle | Wei, Yifeng Funk, Michael Andrew Rosado, Leonardo A. Baek, Jiyeon Stubbe, JoAnne Drennan, Catherine L The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant |
| title | The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant |
| title_full | The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant |
| title_fullStr | The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant |
| title_full_unstemmed | The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant |
| title_short | The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant |
| title_sort | class iii ribonucleotide reductase from neisseria bacilliformis can utilize thioredoxin as a reductant |
| url | http://hdl.handle.net/1721.1/95768 https://orcid.org/0000-0001-5486-2755 https://orcid.org/0000-0002-8683-3593 https://orcid.org/0000-0001-8076-4489 |
| work_keys_str_mv | AT weiyifeng theclassiiiribonucleotidereductasefromneisseriabacilliformiscanutilizethioredoxinasareductant AT funkmichaelandrew theclassiiiribonucleotidereductasefromneisseriabacilliformiscanutilizethioredoxinasareductant AT rosadoleonardoa theclassiiiribonucleotidereductasefromneisseriabacilliformiscanutilizethioredoxinasareductant AT baekjiyeon theclassiiiribonucleotidereductasefromneisseriabacilliformiscanutilizethioredoxinasareductant AT stubbejoanne theclassiiiribonucleotidereductasefromneisseriabacilliformiscanutilizethioredoxinasareductant AT drennancatherinel theclassiiiribonucleotidereductasefromneisseriabacilliformiscanutilizethioredoxinasareductant AT weiyifeng classiiiribonucleotidereductasefromneisseriabacilliformiscanutilizethioredoxinasareductant AT funkmichaelandrew classiiiribonucleotidereductasefromneisseriabacilliformiscanutilizethioredoxinasareductant AT rosadoleonardoa classiiiribonucleotidereductasefromneisseriabacilliformiscanutilizethioredoxinasareductant AT baekjiyeon classiiiribonucleotidereductasefromneisseriabacilliformiscanutilizethioredoxinasareductant AT stubbejoanne classiiiribonucleotidereductasefromneisseriabacilliformiscanutilizethioredoxinasareductant AT drennancatherinel classiiiribonucleotidereductasefromneisseriabacilliformiscanutilizethioredoxinasareductant |